PubMed Health⌕ Search

Biomedical subjects

A Borgström

Publications and source records attributed to A Borgström.

At least 73 records · Page 4Linked to original sources
PubMed1989

Patterns of immunoreactive trypsin in serum from patients with acute abdominal disorders.

Immunoreactive trypsin in serum can be divided into trypsinogen and trypsin-alpha 1-proteinase inhibitor (alpha 1PI) complexes. These were studied separately in serum from 204 patients with acute gastro-intestinal symptoms. Elevated levels of both trypsinogen and trypsin-alpha 1PI complexes were seen in patients with acute pancreatitis. Elevated levels of trypsinogen and normal or slightly elevated levels of trypsin-alpha 1PI complexes were seen in patients with biliary tract diseases. An isolated increase in the concentration of trypsin-alpha 1PI complexes with normal trypsinogen and amylase levels were seen in patients with perforated ulcer. This third cluster may result from an absorption of active trypsin from the peritoneal cavity. Small amounts of trypsin-alpha 1PI complexes were present also in serum from patients free from pancreatic disease. The results in this study show that high levels of trypsin-alpha 1PI complexes in serum are seen mainly in patients with acute pancreatitis. However, elevated levels are also seen in other pathological conditions in the upper gastrointestinal tract; therefore an assay for these complexes is not a specific diagnostic test for acute pancreatitis.

Abdomen, Acute↗
PubMed1989

Local administration of human pancreatic secretory trypsin inhibitor prevents the development of experimental acute pancreatitis in rats and dogs.

The objective of this investigation was to test the capacity of recombinant human pancreatic secretory trypsin inhibitor (rhPSTI) to provide prophylaxis against experimental pancreatitis. Acute hemorrhagic pancreatitis was induced by intraductal injection of sodium taurocholate in rats and by intraductal injection of bile in dogs. In one treatment group of rats the injection of taurocholate was preceded by injection of rhPSTI. In a second group of rats the rhPSTI was given intraperitoneally starting 15 min after the induction of acute pancreatitis. The survival rate in a control group of rats was 13%. In contrast, the survival rate in groups receiving rhPSTI intraductally or intraperitoneally was 80% and 63%, respectively. The survival rate in a control group of dogs was 40% at 24 h and 0% at 48 h. In contrast, all the dogs receiving a single intraductal dose of rhPSTI, either immediately before the bile injection or mixed with the bile, survived for up to 6 weeks. Detailed biochemical and immunohistologic studies in the dog indicate that, whereas rhPSTI cannot prevent the initial bile-induced injury, it does prevent the subsequent development of that injury to the point where there is massive damage to the pancreas and the surrounding tissues, and changes in blood chemistry. The development of the initial injury is, therefore, presumed to involve activation of trypsinogen. Since rhPSTI prevents the serious consequences of experimental pancreatic injury by blocking the action of trypsin, and since the pathobiochemistry of human acute pancreatitis also implies an important role for trypsin, it is possible that rhPSTI could protect humans from the pancreatitis that complicates endoscopic retrograde cholangiopancreatography and endoscopic papillotomy.

Acute Disease↗
PubMed1989

Effect of chemotherapy on dental maturity in children with hematological malignancies.

Dental maturity or dental age was determined in 44 children with hematological malignancies treated with chemotherapy. No significant difference was observed between the chronological and dental age in children treated with chemotherapy compared to healthy controls. With regard to the number of erupted permanent teeth, no significant differences could be found between the two groups. The results indicate that chemotherapy given to children with hematological malignancies did not interfere with dental maturity or eruption of permanent teeth.

Adolescent↗
PubMed1988

Interactions in vitro and in vivo between anionic and cationic porcine trypsin and porcine plasma proteinase inhibitors.

A method for purifying porcine anionic and cationic trypsin is presented. Reaction mixtures with increasing amounts of the two porcine trypsins and porcine serum were studied in vitro to evaluate the relative importance of alpha 1-macroglobulin and alpha 2-macroglobulin as well as alpha 1-proteinase inhibitor in the rapid binding of porcine anionic and cationic trypsin. Porcine cationic trypsin was preferentially bound to alpha 1-macroglobulin, while anionic trypsin exhibited equal binding to both alpha-macroglobulins. Both trypsins were also bound by the alpha 1-proteinase inhibitor but not until alpha 1-macroglobulin approached saturation. Trypsin-alpha-macroglobulin complexes were cleared from plasma with a half-life of 6 min. For trypsin-alpha 1-proteinase inhibitor-complexes the half-life was 120 min. These findings are in accordance with results for other mammalian species, including man.

Animals↗
PubMed1987

Protamine reversal of anticoagulation achieved with a low molecular weight heparin. The effects on eicosanoids, clotting and complement factors.

Hemodynamic and hematologic effects of protamine reversal of low molecular weight heparin (LMWH) anticoagulation with and without protamine pretreatment, as well as reversal of anticoagulation with unfractionated standard heparin (SH), were studied in canine subjects. Protamine reversal caused less severe thrombocytopenia in the two LMWH groups compared to SH animals, while neutropenia occurred equally in all groups. Cl-esterase inhibitor levels were minimally increased, whereas C3 levels and leucotriene levels were unaltered. TxB2 and 6-keto-PGF1 alpha increased during protamine reversal of LMWH anticoagulation. TCT and APTT were affected less with LMWH than SH anticoagulation. Anti-Xa levels increased with anticoagulation in all animals, but protamine did not reverse the elevated anti-Xa levels in LMWH anticoagulated dogs to the same degree as occurred with SH anticoagulation. TCT, APTT and bleeding times were normalized by protamine in all animals. Protamine reversal of LMWH anticoagulation with or without protamine pretreatment did not reveal any clear differences in eicosanoids or complement factors compared to SH anticoagulation, although differences in anti-Xa activity clearly separated these two heparins.

Animals↗
PubMed1987

Haemodynamic and haematologic alterations with protamine reversal of anticoagulation: comparison of standard heparin and a low molecular weight heparin fragment.

Reversal of anticoagulation with protamine sulfate causes many adverse haemodynamic and haematologic effects which could be due to differences in the mechanism of action of standard and low molecular weight heparin. Three groups of dogs were investigated: one group received normal saline pretreatment followed by heparinisation with standard heparin 150 IU/kg followed by protamine sulfate reversal 1.5 mg/kg after aortic interposition grafting: the second group were given normal saline pretreatment followed by heparinisation with low molecular weight heparin 150 U antiXa/kg and after grafting protamine sulfate reversal 1.5 mg/kg. The third group were given protamine sulfate pretreatment 2.25 mg/kg followed by low molecular weight heparin 150 U antiXa/kg and later protamine sulfate reversal 1.5 mg/kg after grafting. The same haemodynamic changes were seen regardless of the type of heparin or pretreatment with protamine given along with low molecular weight heparin. There was a suggestion that regular heparin cause a more pronounced increase in pulmonary artery pressure and a decrease in heart rate. On the other hand the systemic hypotension and reduction of cardiac output seemed more pronounced in the low molecular weight heparin group. Platelet count decreased less in the low molecular weight heparin group, but white blood cell count was equally reduced. Pretreatment with protamine did not abolish the adverse effects of protamine when reversing anticoagulation achieved with low molecular weight heparin, a finding not shared with standard heparin-protamine interactions.

Animals↗
PubMed1986

Serum levels of immunoreactive PSTI in acute abdominal disorders, with special reference to a possible extrapancreatic PSTI production.

The concentration of the pancreatic secretory trypsin inhibitor (PSTI) was measured in serum from 360 patients with acute abdominal diseases. Elevated levels were found in acute pancreatitis, cholangitis, choledocholithiasis, acute cholecystitis, pancreatic pseudocyst, malignancy, renal failure and in several different inflammatory conditions not connected with the pancreas. The results suggest the possibility of an extra-pancreatic production of PSTI, especially since the changes seen over time do not favour leakage or reabsorption as the cause of the high PSTI levels seen in acute pancreatitis. PSTI rather behaves as an acute phase reactant, as judged from the parallelism in the reaction pattern with antichymotrypsin.

Acute Disease↗
PubMed1986

Pancreatic endoproteases and pancreatic secretory trypsin inhibitor immunoreactivity in human Paneth cells.

Normal and metaplastic gastrointestinal mucosa obtained at surgical resection were studied by light microscopy, using the unlabelled antibody enzyme method for immunohistochemical staining of lysozyme, pancreatic endoproteases, and pancreatic secretory trypsin inhibitor (PSTI). Paneth cells in the mucosa of normal small intestine, gastric mucosa with intestinal metaplasia, and colonic metaplastic mucosa were found to contain anionic trypsin, cationic trypsin, lysozyme, and PSTI immunoreactivity, but not chymotrypsin and elastase immunoreactivity. Normal gastric and colonic mucosa and some goblet cells in the small intestine showed positive PSTI immunoreactivity but no endoprotease immunoreactivity. The presence of immunoreactive trypsin and immunoreactive PSTI in the Paneth cells, which are of secretory type, probably indicates an important extrapancreatic source of these proteins rather than a storage of endocytosed material.

Adenoma↗
PubMed1986

Metabolism of 131I-labelled human pancreatic cationic trypsin after intraduodenal administration.

Human pancreatic cationic trypsin labelled with 131I was administered into the duodenum in 9 healthy individuals. Five had earlier been proctocolectomized and had ileostomies. Radioactivity was measured in plasma, urine, ileostomy content and feces for a period of 72 h. Radioactivity was present in plasma 15 min after administration. The total recovery of radioactivity was 78-98%, the largest amount being observed in urine during the first 24-hour period. About 20% of the administered radioactive dose was recovered in ileostomy content and 10% in feces. The recovered radioactivity in plasma, urine and extracts of ileostomy content and feces was characterized with dialysis and gel filtration. All radioactivity in plasma and urine corresponded to free 131I, whereas in the extracts radioactivity corresponding to intact enzyme and degradation products as well as a small amount of free 131I was observed. It is concluded that pancreatic trypsin is degraded during intestinal passage as with other proteins. Due to a deiodinating mechanism in the intestine, only free 131I is absorbed into the circulation. This deiodination does not take place in duodenal juice. The absence of high molecular weight radioactivity in plasma argues against an enteropancreatic circulation.

Adult↗
PubMed1986

Elevated pancreatic secretory trypsin inhibitor levels during severe inflammatory disease, renal insufficiency, and after various surgical procedures.

Elevated levels of immunoreactive pancreatic secretory trypsin inhibitor (PSTI) were found in serum from patients with perforated duodenal ulcer, bacterial peritonitis, urosepticemia, pneumonia, acute renal failure, and also after different surgical procedures. The extent of the trauma seemed to determine the maximal level of PSTI. The increase found paralleled the changes seen in the acute-phase protein antichymotrypsin. There was, however, almost no increase in trypsinogen, thought to be produced together with PSTI in the acinar cells of the pancreas. In conclusion, there is evidence that PSTI is probably also produced somewhere outside the pancreas, in agreement with recent immunohistochemical data. This production may be part of a general acute-phase reaction. Thus, PSTI may have a more general inhibitory function against trypsin-like protease release in tissue injury, instead of being a purely local trypsin inhibitor in the pancreatic gland.

Acute Kidney Injury↗
PubMed1986

Characterization of radioactivity in plasma after intraduodenal administration of 131I-labelled human cationic trypsin.

Active human pancreatic cationic trypsin labelled with 131I was administered into the duodenum in nine healthy individuals pretreated with "cold", i.e. non-radioactive iodine. Radioactivity in plasma was measured during 72 hours and was present in plasma after 15 minutes with a maximum 1 hour after administration. The recovered radioactivity in plasma was characterized using dialysis and gel-filtration and the radioactive iodine was found to be in the form of free 131I. Our results are in agreement with recent experimental studies indicating the presence of de-iodinases in the intestine. Furthermore, it was found that pretreatment with "cold" iodine prevented isotope binding to circulating plasma proteins.

Adult↗
PubMed1986

Immunoreactive anionic and cationic trypsins in serum after experimental porcine pancreatic transplantation.

Immunoreactive anionic and cationic trypsins (irAT and irCT) were measured in blood samples taken daily from 20 pigs during 60 days after whole organ pancreatic transplantation. Immunosuppression was discontinued on the twenty-eighth day after transplantation. IrAT concentrations showed three distinct peaks, the first immediately after operation, the second around the seventh day after operation, and the third irAT peak was seen 2 to 9 days after discontinuation of immunosuppression therapy. IrCT levels paralleled the irAT levels only in the first peak immediately after transplantation. After this there was a dissociation between the concentrations of the two immunoreactive trypsins, with low irCT levels and high irAT levels. Increased irAT levels heralded rejection of the pancreatic allograft by 4 to 30 days (median 20 days) in 13 of the 16 rejecting animals (80%). In addition, low irCT levels preceded hyperglycemia in 13 of the 16 rejecting pigs by 2 to 47 days (median 21 days). The first postoperative peak of immunoreactive trypsins is thought to be related to the operative and storage trauma, whereas the second and third peaks are thought to reflect a rejection process. The results suggest that immunoreactive trypsins can be used as markers for pancreatic allograft rejection.

Animals↗
PubMed1985

Plasma fibronectin in relation to surgical trauma.

Plasma concentrations of fibronectin, alpha 2-macroglobulin and orosomucoid were monitored immunochemically in 20 patients before, during and after surgery. At 2 h after the induction of anaesthesia fibronectin concentrations were lowered 31 +/- 6% (SEM) compared to values obtained 1-3 d preoperatively. However, the fibronectin concentration decreased 17 +/- 5% (SEM) compared to preoperative values at the beginning of surgery. Most of the decline was thus not caused by the operative trauma. The perioperative changes in fibronectin concentrations did not differ from those found in alpha 2-macroglobulin and, up to 2 h postoperatively, orosomucoid.

Fibronectins↗
PubMed1984

Fate of intravenously injected trypsin in dog with special reference to the existence of an enteropancreatic circulation.

In 3 mongrel dogs the pancreatic duct and bile duct were cannulated. After intravenous injection of 125I-labelled anionic dog trypsin bile, pancreatic juice and blood samples were collected during 3 h. 125I-trypsin is eliminated from the circulation in dogs with a half time of 15 min. Only 0.15% of the radioactivity is secreted in the pancreatic juice and 0.75% in the bile during 3 h. 10% of the radioactivity in pancreatic juice is protein bound and 45% in the bile is protein bound. The results argue against biologically significant enteropancreatic circulation of trypsin in dogs.

Animals↗